THE EFFECT OF FENTON'S REAGENT ON TRYPSIN AND RIBONUCLEASE.

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Abstract:

The inactivation of trypsin by Fentons reagent is very fast during the first few minutes of reaction in the first three minutes of reaction about 50 of the activity is lost. However, the inactivation after this initial reaction period is much slower. Fractionation of the reaction mixture shows the presence of two main components a fast fraction with little activity and a slower and more active fraction. Several authors have published experiments showing that partially damaged molecules are formed during the irradiation of proteins. It was possible to demonstrate that this is also true for trypsin treated with Fentons reagent. Furthermore, trypsin after suffering this double treatment showed marked changes in its enzymatic characteristics. Cu was found to have a marked influence on the inactivation of ribonuclease by Fentons reagent.

Author(s):
Perrone, J. C.
Author Organization(s):
INSTITUTO NACIONAL DE TECNOLOGIA RIO DE JANEIRO (BRAZIL)
Descriptive Note:
Final rept. no. 2, 1 Jun 65-31 May 66.
Pagination:
0038

Security Markings

DOCUMENT & CONTEXTUAL SUMMARY

Distribution:
Approved For Public Release

RECORD

Collection: TR
Identifying Numbers
Contract/Grant Number(s):
DA-ARO-49-092-65-G82, DA-ARO-49-092-64-G49
Project Number(s):
DA-2N014501B71D-00-008-LA
 Subject Terms
Communities of Interest:
No COI(s) Identified
Descriptor(s):
*TRYPSIN, *RIBONUCLEASE, ENZYME INHIBITORS, REACTION KINETICS, ELECTROPHORESIS, CHROMATOGRAPHIC ANALYSIS, AMINO ACIDS, RADIATION EFFECTS, COPPER, DECOMPOSITION, THERMAL STABILITY, HYDROGEN PEROXIDE, BRAZIL
Field(s)/Group(s):
Biochemistry
Report Date:
1966 Jun 01